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Nature Cell Biology
Chaperoning the nuclear envelope
Jill Bouchard
Editor in Chief, Condensates.com
Here's the News & Views article about the 2 recent articles in Nat Cell Biol about the chaperones and the nuclear pore complex. See the first paper about the DNAJB6 chaperone and the NPC. See the second paper about aberrant condensates that sequester chaperones.
Nature Cell Biology
Atypical nuclear envelope condensates linked to neurological disorders reveal nucleoporin-directed chaperone activities
Nature cell biology
The chaperone DNAJB6 surveils FG-nucleoporins and is required for interphase nuclear pore complex biogenesis
Nature Communications
A simple thermodynamic description of phase separation of Nup98 FG domains
BioEssays : news and reviews in molecular, cellular and developmental biology
Importin α/β and the tug of war to keep TDP-43 in solution: quo vadis?
bioRxiv
Barrier-properties of Nup98 FG phases ruled by FG motif identity and inter-FG spacer length
Clinical lymphoma, myeloma & leukemia
AML-158 Phase Separation Mediates NUP98 Fusion Oncoprotein Leukemic Transformation
bioRxiv
Peroxisome biogenesis initiated by protein phase separation
bioRxiv
Liquid-liquid phase separation of intrinsically disordered FG-Nups is driven by highly-dynamic hydrophobic FG-motifs
Frontiers in plant science
Nuclear dynamics: Formation of bodies and trafficking in plant nuclei
bioRxiv
Multiple mechanisms prevent ectopic condensation of FG nucleoporins in the cytoplasm
Array
Must ReadVIDEO: Ankur Jain on Nucleic Acid Phase Separation
bioRxiv
A simple thermodynamic description of phase separation of Nup98 FG domains
Physics reports
Physics of the Nuclear Pore Complex: Theory, Modeling and Experiment
Trends in Cell Biology
Interphase microtubules in nuclear organization and genome maintenance
bioRxiv
Deciphering the conformations and dynamics of FG-nucleoporins in situ
bioRxiv
Nuclear architecture protein Distal antenna balances genome-binding and phase-separation properties to regulate neuroblast competence
Protein science : a publication of the Protein Society
A unified statistical potential reveals that amino acid stickiness governs nonspecific recruitment of client proteins into condensates
Nature Communications